Evidence map›Paper›PMID 25862165›Full record

ArticleSmall GTPases2015

Integration of the Rac1- and actin-binding properties of Coronin-1C.

Frances C Tilley, Rosalind C Williamson, Paul R Race, Thomas C Rendall, Mark D Bass

Abstract readLetter
In one paragraph

Article in Small GTPases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Frances C Tilleya School of Biochemistry; University of Bristol ; Bristol , UK.
Rosalind C Williamson
Paul R Race
Thomas C Rendall
Mark D Bass

Funding

Wellcome Trust 088419
6 · The paper itself

Abstract

The coronin family of actin-binding proteins regulate actin branching by inhibiting Arp2/3. We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that proposed for other coronins. Through these interactions coronin-1C redistributes Rac1 from the back of the cell to the leading edge for either activation or sequestration by the associated Rac1-inhibitor, RCC2. Here we investigate the relationship between the Rac1- and actin-binding properties of coronin-1C and find that, although actin appears to be involved in the retrafficking of Rac1, signaling by Rac1 lies upstream of the stress fiber-formation, for which the coronins were originally characterized.

Indexed as

ActinsAmino Acid SequenceAnimalsHumansMiceMicrofilament ProteinsMolecular Sequence DataProtein BindingProtein Transportrac1 GTP-Binding ProteinSequence AlignmentActinscoronin proteinsMicrofilament Proteinsrac1 GTP-Binding ProteinactinCoronin-1CCRIB: Cdc42/Rac-interacting binding domainECM: extracellular matrixendocytosisGEF: guanine nucleotide exchange factorPAK: p21-activated kinaseRac1trafficking

Identifiers

PMID25862165
PMCPMC4601492

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.